Prothrombin activation by a metalloprotease from Staphylococcus aureus.
Formation of thrombin during incubation of purified bovine prothrombin with purified staphylococcal metalloprotease has been investigated. Thrombin activity was estimated by examination of clotting time and by digestion of a synthetic substrate, Chromozym TH. The metalloprotease caused direct activation of prothrombin which was inhibited by the addition of ethylenediaminetetraacetic acid. Metalloprotease produced by some strains of Staphylococcus aureus may simulate staphylocoagulase activity.
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D002417:Cattle; D002474:Cell-Free System; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism* / Q000494:pharmacology; D008666:Metalloendopeptidases; D011516:Prothrombin / Q000378:metabolism* / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000201:enzymology*; D013917:Thrombin / Q000096:biosynthesis; D014757:Viper Venoms / Q000494:pharmacology
D014757:Viper Venoms; D011516:Prothrombin; D004492:Edetic Acid; D010450:Endopeptidases; D013917:Thrombin; D008666:Metalloendopeptidases; C020097:ecarin